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Protein

Proteasome subunit alpha type-1

Gene

SCL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteasomal ubiquitin-independent protein catabolic process Source: SGD
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciYEAST:G3O-30533-MONOMER.
ReactomeiREACT_291351. Orc1 removal from chromatin.
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_343770. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_344477. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_346191. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_347103. ER-Phagosome pathway.
REACT_354180. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1 (EC:3.4.25.1)
Alternative name(s):
Macropain subunit C7-alpha
Multicatalytic endopeptidase complex C7
Proteasome component C7-alpha
Proteasome component Y8
Proteinase YSCE subunit 7
SCL1 suppressor protein
Gene namesi
Name:SCL1
Synonyms:PRC2, PRS2
Ordered Locus Names:YGL011C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL011c.
SGDiS000002979. SCL1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nuclear outer membrane-endoplasmic reticulum membrane network Source: SGD
  3. nucleus Source: SGD
  4. proteasome core complex, alpha-subunit complex Source: SGD
  5. proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 252251Proteasome subunit alpha type-1PRO_0000124141Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei237 – 2371Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP21243.
PaxDbiP21243.
PeptideAtlasiP21243.
PRIDEiP21243.

2D gel databases

UCD-2DPAGEP21243.

Expressioni

Gene expression databases

GenevestigatoriP21243.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with CIC1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PRE10P212426EBI-13975,EBI-13963
PRE8P236396EBI-13975,EBI-13959

Protein-protein interaction databases

BioGridi33235. 77 interactions.
DIPiDIP-2810N.
IntActiP21243. 28 interactions.
MINTiMINT-525412.

Structurei

Secondary structure

1
252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 144Combined sources
Beta strandi16 – 183Combined sources
Turni21 – 233Combined sources
Helixi26 – 349Combined sources
Turni35 – 384Combined sources
Beta strandi42 – 465Combined sources
Beta strandi48 – 569Combined sources
Beta strandi62 – 643Combined sources
Helixi66 – 683Combined sources
Beta strandi71 – 744Combined sources
Beta strandi76 – 783Combined sources
Beta strandi80 – 856Combined sources
Helixi87 – 10822Combined sources
Helixi114 – 13017Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi140 – 1478Combined sources
Turni148 – 1503Combined sources
Beta strandi151 – 1577Combined sources
Turni159 – 1613Combined sources
Beta strandi163 – 17210Combined sources
Helixi175 – 18915Combined sources
Beta strandi191 – 1933Combined sources
Helixi199 – 21416Combined sources
Beta strandi222 – 2298Combined sources
Beta strandi232 – 2354Combined sources
Helixi238 – 24811Combined sources
Turni249 – 2513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20A/O1-252[»]
1G0UX-ray2.40G/U1-252[»]
1G65X-ray2.25G/U10-252[»]
1JD2X-ray3.002/G10-252[»]
1RYPX-ray1.90A/O10-252[»]
1Z7QX-ray3.22A/O1-252[»]
2F16X-ray2.80G/U10-252[»]
2FAKX-ray2.80G/U10-252[»]
2GPLX-ray2.81G/U10-252[»]
2ZCYX-ray2.90G/U1-252[»]
3BDMX-ray2.70G/U1-252[»]
3D29X-ray2.60G/U12-252[»]
3DY3X-ray2.81G/U10-252[»]
3DY4X-ray2.80G/U10-252[»]
3E47X-ray3.00G/U10-252[»]
3GPJX-ray2.70G/U10-252[»]
3GPTX-ray2.41G/U10-252[»]
3GPWX-ray2.50G/U10-252[»]
3HYEX-ray2.50G/U10-252[»]
3MG0X-ray2.68G/U10-252[»]
3MG4X-ray3.11G/U10-252[»]
3MG6X-ray2.60G/U1-252[»]
3MG7X-ray2.78G/U1-252[»]
3MG8X-ray2.59G/U1-252[»]
3NZJX-ray2.40G/U1-252[»]
3NZWX-ray2.50G/U1-252[»]
3NZXX-ray2.70G/U1-252[»]
3OEUX-ray2.60G/U10-252[»]
3OEVX-ray2.85G/U10-252[»]
3OKJX-ray2.70G/U10-252[»]
3SDIX-ray2.65G/U10-252[»]
3SDKX-ray2.70G/U10-252[»]
3SHJX-ray2.80G/U10-252[»]
3TDDX-ray2.70G/U10-252[»]
3UN4X-ray3.40G/U1-252[»]
3UN8X-ray2.70G/U1-252[»]
3WXRX-ray3.15A/O1-252[»]
4CR2electron microscopy7.70A1-252[»]
4CR3electron microscopy9.30A1-252[»]
4CR4electron microscopy8.80A1-252[»]
4EU2X-ray2.51A/O10-250[»]
4FZCX-ray2.80G/U10-252[»]
4FZGX-ray3.00G/U10-252[»]
4G4SX-ray2.49A1-252[»]
4GK7X-ray2.80G/U10-252[»]
4HNPX-ray2.80G/U10-252[»]
4HRCX-ray2.80G/U10-252[»]
4HRDX-ray2.80G/U10-252[»]
4INRX-ray2.70G/U1-252[»]
4INTX-ray2.90G/U1-252[»]
4INUX-ray3.10G/U1-252[»]
4J70X-ray2.80G/U1-252[»]
4JSQX-ray2.80G/U1-252[»]
4JSUX-ray2.90G/U1-252[»]
4JT0X-ray3.10G/U1-252[»]
4LQIX-ray2.70G/U10-252[»]
4LTCX-ray2.50G/U1-252[»]
4NNNX-ray2.50G/U1-252[»]
4NNWX-ray2.60G/U1-252[»]
4NO1X-ray2.50G/U1-252[»]
4NO6X-ray3.00G/U1-252[»]
4NO8X-ray2.70G/U1-252[»]
4NO9X-ray2.90G/U1-252[»]
4Q1SX-ray2.60G/U1-252[»]
4QBYX-ray3.00G/U1-252[»]
4QLQX-ray2.40G/U1-252[»]
4QLSX-ray2.80G/U1-252[»]
4QLTX-ray2.80G/U1-252[»]
4QLUX-ray2.80G/U1-252[»]
4QLVX-ray2.90G/U1-252[»]
4R02X-ray2.50G/U1-252[»]
4R17X-ray2.10G/U1-252[»]
4R18X-ray2.40G/U1-252[»]
4RURX-ray2.50G/U1-252[»]
4V7OX-ray3.00AA/AC/BA/BO10-252[»]
ProteinModelPortaliP21243.
SMRiP21243. Positions 10-252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21243.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074807.
HOGENOMiHOG000091084.
InParanoidiP21243.
KOiK02730.
OMAiRMANINQ.
OrthoDBiEOG7SBP0C.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21243-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGAAAASAA GYDRHITIFS PEGRLYQVEY AFKATNQTNI NSLAVRGKDC
60 70 80 90 100
TVVISQKKVP DKLLDPTTVS YIFCISRTIG MVVNGPIPDA RNAALRAKAE
110 120 130 140 150
AAEFRYKYGY DMPCDVLAKR MANLSQIYTQ RAYMRPLGVI LTFVSVDEEL
160 170 180 190 200
GPSIYKTDPA GYYVGYKATA TGPKQQEITT NLENHFKKSK IDHINEESWE
210 220 230 240 250
KVVEFAITHM IDALGTEFSK NDLEVGVATK DKFFTLSAEN IEERLVAIAE

QD
Length:252
Mass (Da):28,001
Last modified:May 1, 1991 - v1
Checksum:i5B938C862BC8D7EB
GO

Sequence cautioni

The sequence AAA35020.1 differs from that shown. Reason: Frameshift at position 26. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31430 Genomic DNA. Translation: AAA35020.1. Frameshift.
X56971 Genomic DNA. Translation: CAA40292.1.
M55440 mRNA. Translation: AAA35228.1.
M63641 Genomic DNA. Translation: AAA34909.1.
X56732 Genomic DNA. Translation: CAA40056.1.
S58126 Genomic DNA. Translation: AAD13894.1.
Z72533 Genomic DNA. Translation: CAA96711.1.
BK006941 Genomic DNA. Translation: DAA08087.1.
PIRiS11199. SNBYS1.
RefSeqiNP_011504.3. NM_001180876.3.

Genome annotation databases

EnsemblFungiiYGL011C; YGL011C; YGL011C.
GeneIDi852873.
KEGGisce:YGL011C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31430 Genomic DNA. Translation: AAA35020.1. Frameshift.
X56971 Genomic DNA. Translation: CAA40292.1.
M55440 mRNA. Translation: AAA35228.1.
M63641 Genomic DNA. Translation: AAA34909.1.
X56732 Genomic DNA. Translation: CAA40056.1.
S58126 Genomic DNA. Translation: AAD13894.1.
Z72533 Genomic DNA. Translation: CAA96711.1.
BK006941 Genomic DNA. Translation: DAA08087.1.
PIRiS11199. SNBYS1.
RefSeqiNP_011504.3. NM_001180876.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20A/O1-252[»]
1G0UX-ray2.40G/U1-252[»]
1G65X-ray2.25G/U10-252[»]
1JD2X-ray3.002/G10-252[»]
1RYPX-ray1.90A/O10-252[»]
1Z7QX-ray3.22A/O1-252[»]
2F16X-ray2.80G/U10-252[»]
2FAKX-ray2.80G/U10-252[»]
2GPLX-ray2.81G/U10-252[»]
2ZCYX-ray2.90G/U1-252[»]
3BDMX-ray2.70G/U1-252[»]
3D29X-ray2.60G/U12-252[»]
3DY3X-ray2.81G/U10-252[»]
3DY4X-ray2.80G/U10-252[»]
3E47X-ray3.00G/U10-252[»]
3GPJX-ray2.70G/U10-252[»]
3GPTX-ray2.41G/U10-252[»]
3GPWX-ray2.50G/U10-252[»]
3HYEX-ray2.50G/U10-252[»]
3MG0X-ray2.68G/U10-252[»]
3MG4X-ray3.11G/U10-252[»]
3MG6X-ray2.60G/U1-252[»]
3MG7X-ray2.78G/U1-252[»]
3MG8X-ray2.59G/U1-252[»]
3NZJX-ray2.40G/U1-252[»]
3NZWX-ray2.50G/U1-252[»]
3NZXX-ray2.70G/U1-252[»]
3OEUX-ray2.60G/U10-252[»]
3OEVX-ray2.85G/U10-252[»]
3OKJX-ray2.70G/U10-252[»]
3SDIX-ray2.65G/U10-252[»]
3SDKX-ray2.70G/U10-252[»]
3SHJX-ray2.80G/U10-252[»]
3TDDX-ray2.70G/U10-252[»]
3UN4X-ray3.40G/U1-252[»]
3UN8X-ray2.70G/U1-252[»]
3WXRX-ray3.15A/O1-252[»]
4CR2electron microscopy7.70A1-252[»]
4CR3electron microscopy9.30A1-252[»]
4CR4electron microscopy8.80A1-252[»]
4EU2X-ray2.51A/O10-250[»]
4FZCX-ray2.80G/U10-252[»]
4FZGX-ray3.00G/U10-252[»]
4G4SX-ray2.49A1-252[»]
4GK7X-ray2.80G/U10-252[»]
4HNPX-ray2.80G/U10-252[»]
4HRCX-ray2.80G/U10-252[»]
4HRDX-ray2.80G/U10-252[»]
4INRX-ray2.70G/U1-252[»]
4INTX-ray2.90G/U1-252[»]
4INUX-ray3.10G/U1-252[»]
4J70X-ray2.80G/U1-252[»]
4JSQX-ray2.80G/U1-252[»]
4JSUX-ray2.90G/U1-252[»]
4JT0X-ray3.10G/U1-252[»]
4LQIX-ray2.70G/U10-252[»]
4LTCX-ray2.50G/U1-252[»]
4NNNX-ray2.50G/U1-252[»]
4NNWX-ray2.60G/U1-252[»]
4NO1X-ray2.50G/U1-252[»]
4NO6X-ray3.00G/U1-252[»]
4NO8X-ray2.70G/U1-252[»]
4NO9X-ray2.90G/U1-252[»]
4Q1SX-ray2.60G/U1-252[»]
4QBYX-ray3.00G/U1-252[»]
4QLQX-ray2.40G/U1-252[»]
4QLSX-ray2.80G/U1-252[»]
4QLTX-ray2.80G/U1-252[»]
4QLUX-ray2.80G/U1-252[»]
4QLVX-ray2.90G/U1-252[»]
4R02X-ray2.50G/U1-252[»]
4R17X-ray2.10G/U1-252[»]
4R18X-ray2.40G/U1-252[»]
4RURX-ray2.50G/U1-252[»]
4V7OX-ray3.00AA/AC/BA/BO10-252[»]
ProteinModelPortaliP21243.
SMRiP21243. Positions 10-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33235. 77 interactions.
DIPiDIP-2810N.
IntActiP21243. 28 interactions.
MINTiMINT-525412.

2D gel databases

UCD-2DPAGEP21243.

Proteomic databases

MaxQBiP21243.
PaxDbiP21243.
PeptideAtlasiP21243.
PRIDEiP21243.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL011C; YGL011C; YGL011C.
GeneIDi852873.
KEGGisce:YGL011C.

Organism-specific databases

CYGDiYGL011c.
SGDiS000002979. SCL1.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074807.
HOGENOMiHOG000091084.
InParanoidiP21243.
KOiK02730.
OMAiRMANINQ.
OrthoDBiEOG7SBP0C.

Enzyme and pathway databases

BioCyciYEAST:G3O-30533-MONOMER.
ReactomeiREACT_291351. Orc1 removal from chromatin.
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_343770. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_344477. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_346191. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_347103. ER-Phagosome pathway.
REACT_354180. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

Miscellaneous databases

EvolutionaryTraceiP21243.
NextBioi972505.
PROiP21243.

Gene expression databases

GenevestigatoriP21243.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The suppressor gene scl1+ of Saccharomyces cerevisiae is essential for growth."
    Balzi E., Chen W., Capieaux E., McCusker J.H., Haber J.E., Goffeau A.
    Gene 83:271-279(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits."
    Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A., Tamura T., Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A., Nakanishi S., Ichihara A.
    J. Biol. Chem. 265:16604-16613(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 174-187 AND 189-198.
  3. "Molecular cloning and functional analysis of three subunits of yeast proteasome."
    Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K.
    Mol. Cell. Biol. 11:344-353(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 26786 / X2180-1A.
  4. "The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6 gene, a new member of the genetic network controlling pleiotropic drug resistance."
    Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.
    Yeast 7:287-299(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 46191 / IL125-2B.
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4."
    Jaeger S., Strayle J., Heinemeyer W., Wolf D.H.
    EMBO J. 20:4423-4431(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIC1.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Structure of 20S proteasome from yeast at 2.4-A resolution."
    Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R.
    Nature 386:463-471(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
  14. "Structural basis for the activation of 20S proteasomes by 11S regulators."
    Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P.
    Nature 408:115-120(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
  16. "Crystal structure of the 20 S proteasome:TMC-95A complex: a non-covalent proteasome inhibitor."
    Groll M., Koguchi Y., Huber R., Kohno J.
    J. Mol. Biol. 311:543-548(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
  17. "TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome."
    Groll M., Goetz M., Kaiser M., Weyher E., Moroder L.
    Chem. Biol. 13:607-614(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
  18. "Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding."
    Groll M., Huber R., Potts B.C.M.
    J. Am. Chem. Soc. 128:5136-5141(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
  19. "Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome."
    Groll M., Berkers C.R., Ploegh H.L., Ovaa H.
    Structure 14:451-456(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 10-252 OF COMPLEX WITH THE 20S PROTEASOME.
  20. "Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
    Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
    Mol. Cell 37:728-735(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-252 IN COMPLEX WITH THE PROTEASOME.
  21. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.

Entry informationi

Entry nameiPSA1_YEAST
AccessioniPrimary (citable) accession number: P21243
Secondary accession number(s): D6VUC6, P15708
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 1, 2015
This is version 174 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 15200 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.